Analysis of ATPases of putative secretion operons in the thermoacidophilic archaeon Sulfolobus solfataricus

• Published in: Microbiology (Society for General Microbiology) Vol. 151; no. 3; pp. 763 - 773
• Main Authors: Albers, Sonja-Verena, Driessen, Arnold J. M
• Format: Journal Article
• Language: English
• Published: Reading Soc General Microbiol 01.03.2005; Society for General Microbiology
• Subjects: Adenosine Triphosphatases - genetics; Adenosine Triphosphatases - metabolism; Amino Acid Sequence; Archaeal Proteins - genetics; Archaeal Proteins - metabolism; Bacteriology; Biological and medical sciences; Culture Media; Escherichia coli - enzymology; Escherichia coli - genetics; Fundamental and applied biological sciences. Psychology; Gene Expression Regulation, Archaeal; Genetics; Hot Temperature; Metabolism. Enzymes; Microbiology; Molecular Sequence Data; Operon; Sulfolobus solfataricus; Sulfolobus solfataricus - enzymology; Sulfolobus solfataricus - genetics; Sulfolobus solfataricus - growth & development; Acidophily; Enzyme; Archaeobacteria; Operon; Secretion; Adenosinetriphosphatase; Sequence alignment; Thermophily; Sulfolobus solfataricus; Sulfolobaceae; Enzymatic activity; Bacteria; Hydrolases; Sulfolobales; Reverse transcription polymerase chain reaction; Gram negative bacteria
• ISSN: 1350-0872; 1465-2080
• DOI: 10.1099/mic.0.27699-0

Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9751 NN Haren, The Netherlands Correspondence Arnold J. M. Driessen a.j.m.driessen{at}biol.rug.nl Gram-negative bacteria use a wide variety of complex mechanisms to secrete proteins across their membranes or to assemble secreted proteins into surface structures. As most archaea only possess a cytoplasmic membrane surrounded by a membrane-anchored S-layer, the organization of such complexes might be significantly different from that in Gram-negative bacteria. Five proteins of Sulfolobus solfataricus , SSO0120, SSO0572, SSO2316, SSO2387 and SSO2680, which are homologous to secretion ATPases of bacterial type II, type IV secretion systems and the type IV pili assembly machinery, were identified. The operon structures of these putative secretion systems encoding gene clusters and the expression patterns of the ATPases under different growth conditions were determined, and it was established that all five putative ATPases do show a divalent cation-dependent ATPase activity at high temperature. These results show that the archaeal secretion systems are related to the bacterial secretion systems and might be powered in a similar way. Sequences of primers used to identify specific transcripts are listed in Supplementary Table S1 with the online version of this paper at http://mic.sgmjournals.org .